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Q8NP73 (DAPF_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Diaminopimelate epimerase

Short name=DAP epimerase
EC=5.1.1.7
Gene names
Name:dapF
Ordered Locus Names:Cgl1943, cg2129
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. Involved in the succinylase branch of the diaminopimelate biosynthesis. Ref.3

Catalytic activity

LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate. Ref.3

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1. HAMAP-Rule MF_00197

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00197.

Sequence similarities

Belongs to the diaminopimelate epimerase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlysine biosynthetic process via diaminopimelate

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondiaminopimelate epimerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 277277Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_0000149837

Regions

Region83 – 853Substrate binding By similarity
Region212 – 2132Substrate binding By similarity
Region222 – 2232Substrate binding By similarity

Sites

Active site831Proton donor/acceptor By similarity
Active site2211Proton donor/acceptor By similarity
Binding site151Substrate By similarity
Binding site481Substrate By similarity
Binding site741Substrate By similarity
Binding site1591Substrate By similarity
Binding site1941Substrate By similarity
Site1611Important for catalytic activity By similarity
Site2121Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond83 ↔ 221 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
Q8NP73 [UniParc].

Last modified October 25, 2002. Version 1.
Checksum: 41458032D8C7E9DF

FASTA27729,203
        10         20         30         40         50         60 
MNLTIPFAKG HATENDFIII PDEDARLDLT PEMVVTLCDR RAGIGADGIL RVVKAADVEG 

        70         80         90        100        110        120 
STVDPSLWFM DYRNADGSLA EMCGNGVRLF AHWLYSRGLV DNTSFDIGTR AGVRHVDILQ 

       130        140        150        160        170        180 
ADQHSAQVRV DMGIPDVTGL STCDINGQVF AGLGVDMGNP HLACVVPGLS ASALADMELR 

       190        200        210        220        230        240 
APTFDQEFFP HGVNVEIVTE LEDDAVSMRV WERGVGETRS CGTGTVAAAC AALADAGLGE 

       250        260        270 
GTVKVCVPGG EVEVQIFDDG STLTGPSAII ALGEVQI 

« Hide

References

« Hide 'large scale' references
[1]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]"Identification and characterization of the last two unknown genes, dapC and dapF, in the succinylase branch of the L-lysine biosynthesis of Corynebacterium glutamicum."
Hartmann M., Tauch A., Eggeling L., Bathe B., Mockel B., Puhler A., Kalinowski J.
J. Biotechnol. 104:199-211(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB99336.1.
BX927153 Genomic DNA. Translation: CAF20284.1.
RefSeqNP_601150.1. NC_003450.3.
YP_226185.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NP73.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg2129.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB99336; BAB99336; BAB99336.
CAF20284; CAF20284; cg2129.
GeneID1019900.
KEGGcgb:cg2129.
cgl:NCgl1868.
PATRIC21495890. VBICorGlu203724_1881.

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220467.
KOK01778.
OMAITIEMGT.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR018510. DAP_epimerase_AS.
IPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERPTHR31689. PTHR31689. 1 hit.
PfamPF01678. DAP_epimerase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00652. DapF. 1 hit.
PROSITEPS01326. DAP_EPIMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPF_CORGL
AccessionPrimary (citable) accession number: Q8NP73
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: October 25, 2002
Last modified: July 9, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways